| First Author | Fukushima K | Year | 2002 |
| Journal | J Mol Biol | Volume | 321 |
| Issue | 2 | Pages | 317-27 |
| PubMed ID | 12144788 | Mgi Jnum | J:78352 |
| Mgi Id | MGI:2384254 | Doi | 10.1016/s0022-2836(02)00588-0 |
| Citation | Fukushima K, et al. (2002) Solution structure of the DFF-C domain of DFF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation. J Mol Biol 321(2):317-27 |
| abstractText | DFF45/ICAD has dual functions in the final stage of apoptosis, by acting as both a folding chaperone and a DNase inhibitor of DFF40/CAD. Here, we present the solution structure of the C-terminal domain of DFF45, which is essential for its chaperone-like activity. The structure of this domain (DFF-C) consists of four alpha helices, which are folded in a novel helix-packing arrangement. The 3D structure reveals a large cluster of negatively charged residues on the molecular surface of DFF-C. This observation suggests that charge complementation plays an important role in the interaction of DFF-C with the positively charged catalytic domain of DFF40, and thus for the chaperone activity of DFF45. The structure of DFF-C also provides a rationale for the loss of the chaperone activity in DFF35, a short isoform of DFF45. Indeed, in DFF35, the amino acid sequence is truncated in the middle of the second alpha helix constituting the structure of DFF-C, and thus both the hydrophobic core and the cluster of negative charges are disrupted. |
